Structure of PDB 1p0q Chain A

Receptor sequence
>1p0qA (length=522) Species: 9606 (Homo sapiens) [Search protein sequence]
IIIATKNGKVRGMQLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWS
DIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPK
PKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGF
LALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAAS
VSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCS
RNETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPD
ILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGL
KIFFPGVSEFGKESILFHYTDWVQRPENYREALGDVVGDYNFICPALEFT
KKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDYT
KAEEILSRSIVKRWANFAKYGNPQETQNQSTSWPVFKSTEQKYLTLNTES
TRIMTKLRAQQCRFWTSFFPKV
3D structure
PDB1p0q Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.
ChainA
Resolution2.43 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) G116 G117 G149 S198 A199 Y237 V288 F290 E325 H438
Catalytic site (residue number reindexed from 1) G113 G114 G146 S195 A196 Y234 V284 F286 E321 H432
Enzyme Commision number 3.1.1.8: cholinesterase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FUC A N245 F278 N242 F274
BS02 VXA A G116 G117 S198 A199 H438 G113 G114 S195 A196 H432
Gene Ontology
Molecular Function
GO:0001540 amyloid-beta binding
GO:0003824 catalytic activity
GO:0003990 acetylcholinesterase activity
GO:0004104 cholinesterase activity
GO:0005515 protein binding
GO:0016788 hydrolase activity, acting on ester bonds
GO:0019899 enzyme binding
GO:0033265 choline binding
GO:0042802 identical protein binding
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0006581 acetylcholine catabolic process
GO:0006805 xenobiotic metabolic process
GO:0007584 response to nutrient
GO:0007612 learning
GO:0008285 negative regulation of cell population proliferation
GO:0009410 response to xenobiotic stimulus
GO:0014016 neuroblast differentiation
GO:0016486 peptide hormone processing
GO:0019695 choline metabolic process
GO:0043279 response to alkaloid
GO:0050783 cocaine metabolic process
GO:0050805 negative regulation of synaptic transmission
GO:0051384 response to glucocorticoid
GO:0051593 response to folic acid
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005641 nuclear envelope lumen
GO:0005783 endoplasmic reticulum
GO:0005788 endoplasmic reticulum lumen
GO:0005886 plasma membrane
GO:0072562 blood microparticle

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1p0q, PDBe:1p0q, PDBj:1p0q
PDBsum1p0q
PubMed12869558
UniProtP06276|CHLE_HUMAN Cholinesterase (Gene Name=BCHE)

[Back to BioLiP]